Sorghum protein ingredients: Production, compositional variability and enhancement of aqueous dispersibility through homogenization
Thais Cristina Benatti Gallo,
Valérie Beaumal,
Bérénice Houinsou-Houssou,
Michèle Viau,
Lucie Ribourg-Birault,
Hélène Sotin,
Joëlle Bonicel,
Adeline Boire,
Valéria Aparecida Vieira Queiroz,
Hamza Mameri,
Sylvain Guyot,
Alain Riaublanc,
Vânia Regina Nicoletti,
Claire Berton-Carabin
Affiliations
Thais Cristina Benatti Gallo
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Interfaces et Systèmes Dispersés (ISD), 44316 Nantes cedex 3, France; São Paulo State University (Unesp), Institute of Biosciences, Humanities and Exact Sciences, São José do Rio Preto, Department of Food Engineering and Technology, 15054-000 São José do Rio Preto, São Paulo, Brazil; Corresponding author at: INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Interfaces et Systèmes Dispersés (ISD), 44316 Nantes cedex 3, France.
Valérie Beaumal
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Interfaces et Systèmes Dispersés (ISD), 44316 Nantes cedex 3, France
Bérénice Houinsou-Houssou
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Interfaces et Systèmes Dispersés (ISD), 44316 Nantes cedex 3, France
Michèle Viau
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Interfaces et Systèmes Dispersés (ISD), 44316 Nantes cedex 3, France
Lucie Ribourg-Birault
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Interfaces et Systèmes Dispersés (ISD), 44316 Nantes cedex 3, France
Hélène Sotin
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Polyphénols, Réactivité, Procédés (PRP), 35653 Le Rheu, France
Joëlle Bonicel
INRAE, UMR 1208 Ingénierie des Agropolymères et Technologies Emergentes (IATE), F-34060 Montpellier, France
Adeline Boire
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Interfaces et Systèmes Dispersés (ISD), 44316 Nantes cedex 3, France
Valéria Aparecida Vieira Queiroz
Embrapa Milho e Sorgo, 35701-970 Sete Lagoas, Minas Gerais, Brazil
Hamza Mameri
INRAE, UMR 1208 Ingénierie des Agropolymères et Technologies Emergentes (IATE), F-34060 Montpellier, France
Sylvain Guyot
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Polyphénols, Réactivité, Procédés (PRP), 35653 Le Rheu, France
Alain Riaublanc
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Interfaces et Systèmes Dispersés (ISD), 44316 Nantes cedex 3, France
Vânia Regina Nicoletti
São Paulo State University (Unesp), Institute of Biosciences, Humanities and Exact Sciences, São José do Rio Preto, Department of Food Engineering and Technology, 15054-000 São José do Rio Preto, São Paulo, Brazil
Claire Berton-Carabin
INRAE, UR1268 Biopolymères Interactions Assemblages (BIA), Interfaces et Systèmes Dispersés (ISD), 44316 Nantes cedex 3, France; Wageningen University & Research, Laboratory of Food Process Engineering, 6700 AA Wageningen, the Netherlands
Sorghum protein ingredients show promising applications, given that sorghum is a resilient grain with high protein content and bioactive components, such as tannins, in certain genotypes. This study aimed to investigate the production and characterization of sorghum protein ingredients extracted from both tannin-free and tannin-rich cultivars, along with an examination of their behavior in aqueous suspensions. The use of high-pressure homogenization to improve ingredient dispersibility was also assessed. Protein extracts exhibited protein contents ranging from 50 to 67 g/100 g (wet basis), with the highest values obtained in tannin-free samples. Total lipid contents were between 18 and 26 g/100 g (wet basis), with a high contribution of free fatty acids (68–76 g/100 g lipids), and tocopherol contents ranged from 1080 to 2039 µg/g total lipids. This is substantially higher than the lipid content in flours, implying an accumulation of lipids during the protein extraction process. While the dispersibility of the protein extracts in aqueous media was initially limited, high-pressure homogenization proved effective in reducing the average size of the particles in suspension, from 9–66 µm to 1.8–2.5 µm. This processing step significantly enhanced protein dispersibility by up to 288 %, especially for the tannin-rich samples.